ID IF2_HAHCH Reviewed; 861 AA.
AC Q2SML3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HCH_01239;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; CP000155; ABC28111.1; -; Genomic_DNA.
DR RefSeq; WP_011395184.1; NC_007645.1.
DR AlphaFoldDB; Q2SML3; -.
DR SMR; Q2SML3; -.
DR STRING; 349521.HCH_01239; -.
DR KEGG; hch:HCH_01239; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..861
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335478"
FT DOMAIN 362..531
FT /note="tr-type G"
FT REGION 107..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..378
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 396..400
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 417..420
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 471..474
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 507..509
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 107..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 371..378
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 417..421
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 471..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 861 AA; 93752 MW; 681BBB6A88F27012 CRC64;
MAEVTIKQLA EDVGAPVERL LKQMVDAGLE KRGEGDIVTD SEKQKLLAFL KQSHGESFSE
PKKITLKRKT TTTLKASGTG ANRSINVEVR KKRTYIKRSE AVNDIDAQKQ QDIQRAAEEA
AAKERETEVE VALQNEPGME ATAEVVESVQ QEAANMDTQE AEAAPQASVD ESVSATTAGG
SQEKAGVAAD QEAEDAQKSE ARKTSKHRRN KEDSEVRREP ADAEDLKRRE KHKPKPAPQL
KSSKVIAIEE DDSSEEAPRR ARQRKKKSKV VQDRSVQPIV REVVISDTIT VAELAQKMSV
KGVEVIKRLM GMGIMATLNQ SIDQDVAQLV AEEMGHKVKL LQEDAVETEV LESISFEGES
KSRAPVVSVM GHVDHGKTSL LDYIRRAKVA AQESGGITQH IGAYHVETPR GMISFLDTPG
HAAFTAMRAR GAQCTDIVIL VVAADDGVMP QTQEAVQHAK AAGVPLVVAV NKMDKEQADP
DRVKNELSAL DVIPEEWGGD VQFVPVSAHT GDGIDDLLEA VLLQSEMLEL TAVPDAPGKG
VVIESSLDRG RGSVATVLVQ NGTLRHGDIV LAGEYYGRVR AMVNENGQNV QEAGPSIPVE
ILGLNGTPDA GDEFIVVPDE KKAREVAEFR QNKERQTRLQ RQQAASLENL FENMGKGGVK
ELNIVLKTDV RGSLEALIGA LAEIGNEEVQ VKIIASGVGG ITETDANLAL STQAIIVGFN
VRADASARKI VEKEGIELRY YSVIYNIIDD VKKALTGMLA PEFREDIVGT AEVRDTFKSP
KFGQVAGCMV LEGAVYRNKP IRVLRDNVVI FEGELESLRR FKDDVAEVRA GTECGIGVRN
YEVKVGDIIE VFDKIRVERS L
//
